| UniProt functional annotation for Q9SKE2 | |||
| UniProt code: Q9SKE2. |
| Organism: | Arabidopsis thaliana (Mouse-ear cress). | |
| Taxonomy: | Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. | |
| Function: | Catalyzes the synthesis of jasmonates-amino acid conjugates by adenylation; can use Ile and, in vitro at least, Val, Leu and Phe as conjugating amino acids on jasmonic acid (JA) and 9,10-dihydro-JA substrates, and to a lower extent, on 3-oxo-2-(2Z-pentenyl)- cyclopentane-1-butyric acid (OPC-4) and 12-hydroxy-JA (12-OH-JA). Can synthesize adenosine 5-tetraphosphate in vitro. Required for the JA- mediated signaling pathway that regulates many developmental and defense mechanisms, including growth root inhibition, vegetative storage proteins (VSPs) accumulation, induced systemic resistance (ISR), response to wounding and herbivores, tolerance to ozone O(3) (probably having a role in lesion containment). Plays an important role in the accumulation of JA-Ile in response to wounding, both locally and systemically; promotes JA responding genes especially in distal part of wounded plants, via the JA-Ile-stimulated degradation of JAZ repressor proteins by the SCF(COI)E3 ubiquitin-protein ligase pathway. Involved in the apoptosis-like programmed cell death (PCD) induced by fungal toxin fumonisin B1-mediated (FB1). Required for volatile compounds (C6- aldehydes and allo-ocimene)-mediated defense activation. Involved in the non-pathogenic rhizobacterium-mediated ISR (defense priming) by P.fluorescens (strains CHAOr and WCS417r) and P.putida LSW17S against infection leaf pathogens such as P.syringae pv. tomato and H.parasitica. Required for the JA-dependent resistance to fungi such as P.irregulare, U.vignae and U.appendiculatus. Necessary to induce systemic resistance against R.solanaceraum and P.syringae pv. tomato with P.oligandrum (a non-pathogenic biocontrol agent) cell wall protein fraction (CWP). Mediates PGIP2 accumulation in response to B.cinerea infection and thus contributes to resistance against this pathogen. Modulates the UV-B alteration of leaves attractiveness to diamondback moths P.xylostella leading to insect oviposition. Involved in the regulation of far-red light influence on development, being an actor of the interplay between light and JA signaling (PubMed:28223489). Seems necessary for the salicylic acid (SA)-mediated, NPR1-independent resistance pathway. May contribute to the chitin-elicited pathway. Contributes to the sensitivity toward F.graminearum. {ECO:0000269|PubMed:10921909, ECO:0000269|PubMed:11006337, ECO:0000269|PubMed:11041879, ECO:0000269|PubMed:11041881, ECO:0000269|PubMed:11090217, ECO:0000269|PubMed:11607311, ECO:0000269|PubMed:12084835, ECO:0000269|PubMed:12236603, ECO:0000269|PubMed:12376653, ECO:0000269|PubMed:12509524, ECO:0000269|PubMed:12744510, ECO:0000269|PubMed:12848825, ECO:0000269|PubMed:14558686, ECO:0000269|PubMed:15258265, ECO:0000269|PubMed:15879447, ECO:0000269|PubMed:16639567, ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:17291501, ECO:0000269|PubMed:17601164, ECO:0000269|PubMed:18247047, ECO:0000269|PubMed:19251652, ECO:0000269|PubMed:19304739, ECO:0000269|PubMed:19473329, ECO:0000269|PubMed:20521949, ECO:0000269|PubMed:28223489, ECO:0000269|PubMed:9724702, ECO:0000269|PubMed:9807813}. | |
| Catalytic activity: | Reaction=a jasmonate + an L-alpha-amino acid + ATP = a jasmonyl-L-amino acid + AMP + diphosphate + H(+); Xref=Rhea:RHEA:55772, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:59869, ChEBI:CHEBI:136183, ChEBI:CHEBI:136184, ChEBI:CHEBI:456215; EC=6.3.2.52; Evidence={ECO:0000269|PubMed:18247047}; | |
| Catalytic activity: | Reaction=(+)-7-isojasmonate + ATP + L-isoleucine = AMP + diphosphate + H(+) + L-isoleucine-(+)-7-isojasmonate; Xref=Rhea:RHEA:54812, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045, ChEBI:CHEBI:136179, ChEBI:CHEBI:136180, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15258265}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54813; Evidence={ECO:0000269|PubMed:15258265}; | |
| Activity regulation: | Activated by GSTU20/FIP1. {ECO:0000269|PubMed:28223489}. | |
| Biophysicochemical properties: | Kinetic parameters: KM=0.03 mM for Ile {ECO:0000269|PubMed:18247047}; KM=1.93 mM for Leu {ECO:0000269|PubMed:18247047}; KM=1.84 mM for Phe {ECO:0000269|PubMed:18247047}; KM=2.49 mM for Val {ECO:0000269|PubMed:18247047}; KM=0.19 mM for (-)-JA {ECO:0000269|PubMed:18247047}; Vmax=92.4 nmol/min/mg enzyme with Ile as substrate {ECO:0000269|PubMed:18247047}; Vmax=196.9 nmol/min/mg enzyme with Leu as substrate {ECO:0000269|PubMed:18247047}; Vmax=68.1 nmol/min/mg enzyme with Phe as substrate {ECO:0000269|PubMed:18247047}; Vmax=326.1 nmol/min/mg enzyme with Val as substrate {ECO:0000269|PubMed:18247047}; Vmax=68.8 nmol/min/mg enzyme with (-)-JA as substrate {ECO:0000269|PubMed:18247047}; Vmax=25.38 umol/min/mg enzyme with ATP as substrate (in the presence of JA) {ECO:0000269|PubMed:28223489}; Vmax=59.17 umol/min/mg enzyme with ATP as substrate (in the presence of JA and when in complex with GSTU20/FIP1) {ECO:0000269|PubMed:28223489}; Note=All results obtained at pH 8.6 and 25 degrees Celsius (PubMed:18247047). kcat is 2.72 sec(-1) with ATP as substrate (in the presence of JA). kcat is 6.32 sec(-1) with ATP as substrate (in the presence of JA and when in complex with GSTU20/FIP1) (PubMed:28223489). {ECO:0000269|PubMed:18247047, ECO:0000269|PubMed:28223489}; | |
| Subunit: | Interacts with GSTU20/FIP1 under continuous far red (cFR) light; this binding increases its activity and determines the priority of substrate binding. {ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:28223489}. | |
| Subcellular location: | Cytoplasm {ECO:0000269|PubMed:10921909}. | |
| Induction: | Rapidly induced by auxin. Accumulates locally in response to wounding. {ECO:0000269|PubMed:10921909, ECO:0000269|PubMed:18247047}. | |
| Disruption phenotype: | Long hypocotyl phenotype under continuous far red (cFR) light. Suppression of COP1 disruption. Decreased sensitivity to jasmonic acid (JA) and methyl-jasmonate (MeJA) inhibition of root elongation, but increased sensitivity to abscisic acid during seed germination. Reduced induced systemic resistance (ISR) mediated by P.fluorescens (CHAOr and WCS417r) and P.putida LSW17S in roots toward H.parasitica and P.syringae pv. tomato in leaves. Increased susceptibility to the fungi P.irregulare, U.vignae and U.appendiculatus. Enhanced sensitivity to ozone O(3). Reduced fungal toxin fumonisin B1-mediated (FB1) induced apoptosis-like programmed cell death (PCD). Impaired SA-mediated, NPR1-independent resistance pathway. Reduced gene induction in resposne to chitin. Reduced PGIP2 accumulation upon B.cinerea infection leading to enhanced sensitivity. Altered defense activation by volatile compounds such as C6-aldehydes. Disrupted UV-B alteration of leaves attractiveness to diamondback moths P.xylostella, accompanied with reduced levels of UV-absorbing phenolic compounds. Reduced accumulation of JA-Ile conjugates in response to wounding, both locally and systemically. Compromised P.oligandrum cell wall protein fraction (CWP) induce systemic resistance against R.solanaceraum and P.syringae pv. tomato. Enhanced resistance to F.graminearum. {ECO:0000269|PubMed:10921909, ECO:0000269|PubMed:11006337, ECO:0000269|PubMed:11041879, ECO:0000269|PubMed:11041881, ECO:0000269|PubMed:11090217, ECO:0000269|PubMed:11607311, ECO:0000269|PubMed:12084835, ECO:0000269|PubMed:12236603, ECO:0000269|PubMed:12376653, ECO:0000269|PubMed:12509524, ECO:0000269|PubMed:12744510, ECO:0000269|PubMed:12848825, ECO:0000269|PubMed:14558686, ECO:0000269|PubMed:15879447, ECO:0000269|PubMed:16639567, ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:17601164, ECO:0000269|PubMed:18247047, ECO:0000269|PubMed:19251652, ECO:0000269|PubMed:19304739, ECO:0000269|PubMed:19473329, ECO:0000269|PubMed:20521949, ECO:0000269|PubMed:9724702, ECO:0000269|PubMed:9807813}. | |
| Similarity: | Belongs to the IAA-amido conjugating enzyme family. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.